ID E7G7G7_9FIRM Unreviewed; 640 AA.
AC E7G7G7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=NADH oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9488_00681 {ECO:0000313|EMBL:EFW06042.1};
OS Coprobacillus cateniformis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Coprobacillus.
OX NCBI_TaxID=100884 {ECO:0000313|EMBL:EFW06042.1, ECO:0000313|Proteomes:UP000003157};
RN [1] {ECO:0000313|EMBL:EFW06042.1, ECO:0000313|Proteomes:UP000003157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=29_1 {ECO:0000313|EMBL:EFW06042.1,
RC ECO:0000313|Proteomes:UP000003157};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Sibley C.D.,
RA White A., Strauss J., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Coprobacillus sp. strain 29_1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFW06042.1}.
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DR EMBL; ADKX01000009; EFW06042.1; -; Genomic_DNA.
DR RefSeq; WP_008787797.1; NZ_GL636577.1.
DR AlphaFoldDB; E7G7G7; -.
DR STRING; 100884.GCA_000269565_01026; -.
DR GeneID; 78228908; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_2_9; -.
DR OrthoDB; 9772736at2; -.
DR Proteomes; UP000003157; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02803; OYE_like_FMN_family; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000003157}.
FT DOMAIN 10..323
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 381..604
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 640 AA; 71054 MW; 15AB4C7BED109112 CRC64;
MSFSKKYPHL FEPLQVNQMM IPNRIISAPL GSLTDKSVSG IGMIIRGTSG SVPGPRSRMA
PGSYCFANMQ ESQKVREQVV TIQQRGAKAE FELCHVGQYA YVQPGDYAIG PVGFVREDGI
EVKAMDENMM NEVADAFAKG AVDAKEYGFD MVMLHFGHGW LPTQFLSPHY NKRTDGYGGC
FENRVKIPIQ IVERVRQAVG PDYPLDMRIS GFEYIEDGTP IDEIIRFIQL IEDKIDMVHI
SCGLEREIKA MTKMSSTPYF DHKINVQWSQ KVKEYVHIPV AVVGAIMTPE EAEEILANHQ
ADAVVIGRQI IADPFWTSKA IEEKSEDIVP CLRCMNCYNQ YARNKDRHYG MKSITCCSVN
PRYLHEQSVP AELSKAKTIK KVYVIGGGPA GCKAALTAYE RGHQVILFEK TDVLGGQLSC
SEFDKSKQDL KRYKDYLITQ IHKSSIEVRL QCDALEDIDE IKTGDSLIVA VGAKPISLEI
AGIQQKHVMD ALYAYGHQNE INQKVVIIGG GSIGSELAKL LCHLGKDVTI VEKSEQLCSN
VNEHIQTGLL EKLSECQNLK IFLNSQCLSI QNQSVVIQNN TDLQVIEAQS VIVAVGMQSR
CDIVNQFYGL VPDINVIGDA KRPGTVAQAT HDGYYAGVSL
//